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. 1996 Feb;5(2):357–362. doi: 10.1002/pro.5560050220

BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes.

G Mignogna 1, S Pascarella 1, C Wechselberger 1, C Hinterleitner 1, C Mollay 1, G Amiconi 1, D Barra 1, G Kreil 1
PMCID: PMC2143335  PMID: 8745414

Abstract

From skin secretions of the European frog Bombina bombina, a new peptide has been isolated that contains 60 amino acids, including 10 cysteine residues. Its sequence was determined by automated Edman degradation and confirmed by analysis of the cDNA encoding the precursor. A search in the databanks demonstrated that the pattern of cysteine residues in this skin peptide is similar to the ones found in protease inhibitors from Ascaris and in a segment of human von Willebrand factor. The 3D structure of the trypsin inhibitor from Ascaris suum could be used as a template to build a model of the amphibian peptide. In addition, we have demonstrated that this constituent of skin secretion is indeed an inhibitor of trypsin and thrombin, with K(i) values in the range of 0.1 to 1 microM. The new peptide was thus named BSTI for Bombina skin trypsin/thrombin inhibitor.

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Selected References

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  1. Anastasi A., Erspamer V., Bucci M. Isolation and structure of bombesin and alytesin, 2 analogous active peptides from the skin of the European amphibians Bombina and Alytes. Experientia. 1971 Feb 15;27(2):166–167. doi: 10.1007/BF02145873. [DOI] [PubMed] [Google Scholar]
  2. Ascenzi P., Amiconi G., Coletta M., Lupidi G., Menegatti E., Onesti S., Bolognesi M. Binding of hirudin to human alpha, beta and gamma-thrombin. A comparative kinetic and thermodynamic study. J Mol Biol. 1992 May 5;225(1):177–184. doi: 10.1016/0022-2836(92)91034-m. [DOI] [PubMed] [Google Scholar]
  3. Church G. M., Gilbert W. Genomic sequencing. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991–1995. doi: 10.1073/pnas.81.7.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Darby N. J., Lackey D. B., Smyth D. G. Purification of a cysteine endopeptidase which is secreted with bioactive peptides from the epidermal glands of Xenopus laevis. Eur J Biochem. 1991 Jan 1;195(1):65–70. doi: 10.1111/j.1432-1033.1991.tb15676.x. [DOI] [PubMed] [Google Scholar]
  5. Feinberg A. P., Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. doi: 10.1016/0003-2697(84)90381-6. [DOI] [PubMed] [Google Scholar]
  6. Friedman M., Krull L. H., Cavins J. F. The chromatographic determination of cystine and cysteine residues in proteins as s-beta-(4-pyridylethyl)cysteine. J Biol Chem. 1970 Aug 10;245(15):3868–3871. [PubMed] [Google Scholar]
  7. Frohman M. A., Dush M. K., Martin G. R. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8998–9002. doi: 10.1073/pnas.85.23.8998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gibson B. W., Tang D. Z., Mandrell R., Kelly M., Spindel E. R. Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. J Biol Chem. 1991 Dec 5;266(34):23103–23111. [PubMed] [Google Scholar]
  9. Huang K., Strynadka N. C., Bernard V. D., Peanasky R. J., James M. N. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure. 1994 Jul 15;2(7):679–689. doi: 10.1016/s0969-2126(00)00068-x. [DOI] [PubMed] [Google Scholar]
  10. Kolbe H. V., Huber A., Cordier P., Rasmussen U. B., Bouchon B., Jaquinod M., Vlasak R., Délot E. C., Kreil G. Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins. J Biol Chem. 1993 Aug 5;268(22):16458–16464. [PubMed] [Google Scholar]
  11. Korner J., Chun J., O'Bryan L., Axel R. Prohormone processing in Xenopus oocytes: characterization of cleavage signals and cleavage enzymes. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11393–11397. doi: 10.1073/pnas.88.24.11393. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lazarus L. H., Attila M. The toad, ugly and venomous, wears yet a precious jewel in his skin. Prog Neurobiol. 1993 Oct;41(4):473–507. doi: 10.1016/0301-0082(93)90027-p. [DOI] [PubMed] [Google Scholar]
  13. Luthy J. A., Praissman M., Finkenstadt W. R., Laskowski M., Jr Detailed mechanism of interaction of bovine -trypsin with soybean trypsin inhibitor (Kunitz). I. Stopped flow measurements. J Biol Chem. 1973 Mar 10;248(5):1760–1771. [PubMed] [Google Scholar]
  14. Mignogna G., Simmaco M., Kreil G., Barra D. Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. EMBO J. 1993 Dec;12(12):4829–4832. doi: 10.1002/j.1460-2075.1993.tb06172.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Peanasky R. J., Bentz Y., Homandberg G. A., Minor S. T., Babin D. R. The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the reactive site. Arch Biochem Biophys. 1984 Jul;232(1):135–142. doi: 10.1016/0003-9861(84)90529-0. [DOI] [PubMed] [Google Scholar]
  16. Resnick N. M., Maloy W. L., Guy H. R., Zasloff M. A novel endopeptidase from Xenopus that recognizes alpha-helical secondary structure. Cell. 1991 Aug 9;66(3):541–554. doi: 10.1016/0092-8674(81)90017-9. [DOI] [PubMed] [Google Scholar]
  17. Richter K., Egger R., Kreil G. Molecular cloning of a cDNA encoding the bombesin precursor in skin of Bombina variegata. FEBS Lett. 1990 Mar 26;262(2):353–355. doi: 10.1016/0014-5793(90)80227-a. [DOI] [PubMed] [Google Scholar]
  18. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Simmaco M., Barra D., Chiarini F., Noviello L., Melchiorri P., Kreil G., Richter K. A family of bombinin-related peptides from the skin of Bombina variegata. Eur J Biochem. 1991 Jul 1;199(1):217–222. doi: 10.1111/j.1432-1033.1991.tb16112.x. [DOI] [PubMed] [Google Scholar]
  20. Verweij C. L., Diergaarde P. J., Hart M., Pannekoek H. Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit. EMBO J. 1986 Aug;5(8):1839–1847. doi: 10.1002/j.1460-2075.1986.tb04435.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. WYMAN J., Jr LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. Adv Protein Chem. 1964;19:223–286. doi: 10.1016/s0065-3233(08)60190-4. [DOI] [PubMed] [Google Scholar]
  22. Wechselberger C., Kreil G., Richter K. Isolation and sequence of a cDNA encoding the precursor of a bombesinlike peptide from brain and early embryos of Xenopus laevis. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9819–9822. doi: 10.1073/pnas.89.20.9819. [DOI] [PMC free article] [PubMed] [Google Scholar]

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